| Ultrastructure of the collagen fibril. II. Evidence of the spiral organization of the fibril. | |
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MedLine Citation:
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PMID: 747226 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Unfixed tissue from the human ovary, the tail tendon and skin from the tail of rats are incubated in 5% solutions of uranyl acetate. The collagen fibrils of all tissues are decomposed and display an obvious tridimensional spiral structure on all levels. The fibril is a complex biopolymer constructed out of filaments, surrounded by and associated with an amorphous cementing matrix. The filaments consist of 3 to 5 subfilaments with a thickness of 30--45 A spirally wound around one another. The filaments are twisted along the length of the axis of the fibril under a definite angle of inclination and a pitch of the spiral equal to 1.04--1.12 micrometer for the ovary and from 2.6 to over 5.6 micrometer for the tail tendon. The cross striations seem to spring out of the nodular thickenings along the filaments. Bridge-like connections corresponding to the separate striations are established between adjacent fibrils. A new tridimensional structure model of the collagen fibrils is proposed. |
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Authors:
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R Petkov |
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Publication Detail:
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Type: Journal Article |
Journal Detail:
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Title: Anatomischer Anzeiger Volume: 144 ISSN: 0003-2786 ISO Abbreviation: Anat Anz Publication Date: 1978 |
Date Detail:
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Created Date: 1979-05-23 Completed Date: 1979-05-23 Revised Date: 2004-11-17 |
Medline Journal Info:
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Nlm Unique ID: 0370541 Medline TA: Anat Anz Country: GERMANY, EAST |
Other Details:
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Languages: eng Pagination: 485-501 Citation Subset: IM |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Animals Collagen* Connective Tissue / metabolism, ultrastructure* Female Humans Ovary / ultrastructure Rats Skin / ultrastructure Tail / ultrastructure Tendons / ultrastructure |
| Chemical | |
Reg. No./Substance:
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9007-34-5/Collagen |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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